FMO DATABASE

FMODB ID: ZV3KN

Calculation Name: 4JOI-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4JOI

Chain ID: A

ChEMBL ID:

UniProt ID: Q9H668

Base Structure: X-ray

Registration Date: 2023-09-24

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	141
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1334202.656988
FMO2-HF: Nuclear repulsion	1276478.622075
FMO2-HF: Total energy	-57724.034914
FMO2-MP2: Total energy	-57893.787977

3D Structure

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:24:LEU)

Summations of interaction energy for fragment #1(A:24:LEU)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
0.526	2.303	-0.021	-0.882	-0.873	0.003

Interaction energy analysis for fragmet #1(A:24:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.046 / q_NPA : 0.002

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	26	PHE	0	-0.075	-0.046	3.819	-1.509	0.078	-0.020	-0.869	-0.697	0.003
4	A	27	ALA	0	0.010	0.004	5.924	0.181	0.181	0.000	0.000	0.000	0.000
5	A	28	LYS	1	0.874	0.940	7.341	-0.632	-0.632	0.000	0.000	0.000	0.000
6	A	29	LEU	0	0.044	0.015	9.921	0.093	0.093	0.000	0.000	0.000	0.000
7	A	30	TYR	0	0.040	0.022	12.858	-0.070	-0.070	0.000	0.000	0.000	0.000
8	A	31	ILE	0	-0.026	-0.019	15.696	0.015	0.015	0.000	0.000	0.000	0.000
9	A	32	ARG	1	0.875	0.932	17.299	-0.150	-0.150	0.000	0.000	0.000	0.000
10	A	33	ASP	-1	-0.742	-0.823	14.804	0.320	0.320	0.000	0.000	0.000	0.000
11	A	34	ILE	0	-0.069	-0.038	12.221	-0.005	-0.005	0.000	0.000	0.000	0.000
12	A	35	LEU	0	-0.064	-0.035	14.608	-0.028	-0.028	0.000	0.000	0.000	0.000
13	A	36	ASP	-1	-0.885	-0.932	17.669	0.164	0.164	0.000	0.000	0.000	0.000
14	A	37	MET	0	-0.008	0.031	10.823	0.030	0.030	0.000	0.000	0.000	0.000
15	A	38	LYS	1	0.955	0.982	15.614	-0.163	-0.163	0.000	0.000	0.000	0.000
16	A	39	GLU	-1	-0.839	-0.913	14.050	0.024	0.024	0.000	0.000	0.000	0.000
17	A	40	SER	0	-0.048	-0.013	12.749	0.004	0.004	0.000	0.000	0.000	0.000
18	A	41	ARG	1	0.995	0.971	14.597	-0.043	-0.043	0.000	0.000	0.000	0.000
19	A	42	GLN	0	-0.020	-0.008	15.244	-0.029	-0.029	0.000	0.000	0.000	0.000
20	A	43	VAL	0	-0.021	-0.012	10.619	-0.022	-0.022	0.000	0.000	0.000	0.000
21	A	44	PRO	0	0.044	0.024	12.479	0.008	0.008	0.000	0.000	0.000	0.000
22	A	45	GLY	0	-0.048	-0.023	12.027	-0.045	-0.045	0.000	0.000	0.000	0.000
23	A	46	VAL	0	-0.069	-0.025	7.789	-0.050	-0.050	0.000	0.000	0.000	0.000
24	A	47	PHE	0	0.004	-0.006	9.291	0.004	0.004	0.000	0.000	0.000	0.000
25	A	48	LEU	0	-0.020	-0.005	9.719	0.094	0.094	0.000	0.000	0.000	0.000
26	A	49	TYR	0	-0.023	-0.026	11.194	-0.055	-0.055	0.000	0.000	0.000	0.000
27	A	50	ASN	0	-0.011	-0.003	12.258	0.042	0.042	0.000	0.000	0.000	0.000
28	A	51	GLY	0	-0.003	0.000	13.224	0.024	0.024	0.000	0.000	0.000	0.000
29	A	52	HIS	0	-0.040	-0.026	8.668	0.242	0.242	0.000	0.000	0.000	0.000
30	A	53	PRO	0	-0.032	-0.003	5.734	-0.126	-0.126	0.000	0.000	0.000	0.000
31	A	54	ILE	0	0.008	-0.004	5.586	0.423	0.423	0.000	0.000	0.000	0.000
32	A	55	LYS	1	0.955	0.978	5.042	0.180	0.180	0.000	0.000	0.000	0.000
33	A	56	GLN	0	-0.060	-0.034	4.492	0.241	0.431	-0.001	-0.013	-0.176	0.000
34	A	57	VAL	0	0.078	0.049	5.950	0.392	0.392	0.000	0.000	0.000	0.000
35	A	58	ASP	-1	-0.791	-0.883	8.726	-0.071	-0.071	0.000	0.000	0.000	0.000
36	A	59	VAL	0	0.057	0.033	11.358	0.072	0.072	0.000	0.000	0.000	0.000
37	A	60	LEU	0	-0.029	-0.034	14.844	-0.035	-0.035	0.000	0.000	0.000	0.000
38	A	61	GLY	0	0.042	0.023	18.264	0.018	0.018	0.000	0.000	0.000	0.000
39	A	62	THR	0	0.013	0.016	21.578	-0.014	-0.014	0.000	0.000	0.000	0.000
40	A	63	VAL	0	-0.027	-0.010	23.985	0.001	0.001	0.000	0.000	0.000	0.000
41	A	64	ILE	0	0.038	0.012	25.718	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	65	GLY	0	-0.003	-0.002	27.014	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	66	VAL	0	0.016	0.010	26.778	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	67	ARG	1	0.898	0.951	27.372	0.010	0.010	0.000	0.000	0.000	0.000
45	A	68	GLU	-1	-0.826	-0.896	27.430	-0.041	-0.041	0.000	0.000	0.000	0.000
46	A	69	ARG	1	0.891	0.951	27.664	0.032	0.032	0.000	0.000	0.000	0.000
47	A	70	ASP	-1	-0.829	-0.916	29.239	-0.048	-0.048	0.000	0.000	0.000	0.000
48	A	71	ALA	0	0.001	-0.002	25.421	-0.003	-0.003	0.000	0.000	0.000	0.000
49	A	72	PHE	0	-0.026	-0.015	22.880	-0.009	-0.009	0.000	0.000	0.000	0.000
50	A	73	TYR	0	0.040	0.018	23.816	0.009	0.009	0.000	0.000	0.000	0.000
51	A	74	SER	0	-0.049	-0.018	22.914	-0.004	-0.004	0.000	0.000	0.000	0.000
52	A	75	TYR	0	0.049	0.001	21.807	0.005	0.005	0.000	0.000	0.000	0.000
53	A	76	GLY	0	0.067	0.039	21.987	0.002	0.002	0.000	0.000	0.000	0.000
54	A	77	VAL	0	-0.034	-0.028	19.630	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	78	ASP	-1	-0.842	-0.914	21.661	0.085	0.085	0.000	0.000	0.000	0.000
56	A	79	ASP	-1	-0.723	-0.843	18.545	0.163	0.163	0.000	0.000	0.000	0.000
57	A	80	SER	0	-0.076	-0.030	21.654	0.015	0.015	0.000	0.000	0.000	0.000
58	A	81	THR	0	-0.058	-0.055	20.155	0.009	0.009	0.000	0.000	0.000	0.000
59	A	82	GLY	0	0.004	-0.016	21.470	0.000	0.000	0.000	0.000	0.000	0.000
60	A	83	VAL	0	0.016	0.003	21.992	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	84	ILE	0	0.002	0.008	16.434	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	85	ASN	0	0.020	0.021	20.524	-0.005	-0.005	0.000	0.000	0.000	0.000
63	A	86	CYS	0	-0.021	0.000	17.787	0.001	0.001	0.000	0.000	0.000	0.000
64	A	87	ILE	0	0.004	0.001	18.369	0.000	0.000	0.000	0.000	0.000	0.000
65	A	88	CYS	0	-0.044	-0.020	18.322	-0.020	-0.020	0.000	0.000	0.000	0.000
66	A	89	TRP	0	0.024	0.013	17.677	0.018	0.018	0.000	0.000	0.000	0.000
67	A	90	LYS	1	0.798	0.884	21.573	0.049	0.049	0.000	0.000	0.000	0.000
68	A	91	LYS	1	0.963	0.980	21.472	0.099	0.099	0.000	0.000	0.000	0.000
69	A	92	LEU	0	0.024	0.021	24.316	0.006	0.006	0.000	0.000	0.000	0.000
70	A	112	GLN	0	0.063	0.011	34.750	-0.002	-0.002	0.000	0.000	0.000	0.000
71	A	113	LEU	0	0.072	0.031	32.171	0.002	0.002	0.000	0.000	0.000	0.000
72	A	114	LYS	1	1.007	0.989	33.780	0.052	0.052	0.000	0.000	0.000	0.000
73	A	115	LYS	1	0.889	0.939	36.268	0.037	0.037	0.000	0.000	0.000	0.000
74	A	116	LEU	0	-0.015	0.003	36.094	0.002	0.002	0.000	0.000	0.000	0.000
75	A	117	GLN	0	0.044	0.024	30.760	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	118	GLU	-1	-0.905	-0.934	32.516	-0.048	-0.048	0.000	0.000	0.000	0.000
77	A	119	THR	0	-0.010	-0.013	33.937	0.002	0.002	0.000	0.000	0.000	0.000
78	A	120	ILE	0	0.027	0.014	33.505	0.003	0.003	0.000	0.000	0.000	0.000
79	A	121	GLU	-1	-0.924	-0.960	28.743	-0.055	-0.055	0.000	0.000	0.000	0.000
80	A	122	GLN	0	-0.077	-0.044	31.972	0.005	0.005	0.000	0.000	0.000	0.000
81	A	123	LYS	1	0.890	0.948	34.148	0.020	0.020	0.000	0.000	0.000	0.000
82	A	124	THR	0	0.016	0.009	31.254	0.002	0.002	0.000	0.000	0.000	0.000
83	A	125	LYS	1	0.894	0.947	29.403	0.034	0.034	0.000	0.000	0.000	0.000
84	A	126	ILE	0	-0.025	0.001	23.587	0.002	0.002	0.000	0.000	0.000	0.000
85	A	127	GLU	-1	-0.967	-0.975	27.969	-0.005	-0.005	0.000	0.000	0.000	0.000
86	A	128	ILE	0	-0.045	-0.042	28.920	0.003	0.003	0.000	0.000	0.000	0.000
87	A	129	GLY	0	0.008	0.009	29.060	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	130	ASP	-1	-0.798	-0.885	26.830	0.003	0.003	0.000	0.000	0.000	0.000
89	A	131	THR	0	-0.007	0.007	22.671	0.008	0.008	0.000	0.000	0.000	0.000
90	A	132	ILE	0	-0.003	-0.001	20.164	-0.013	-0.013	0.000	0.000	0.000	0.000
91	A	133	ARG	1	0.817	0.900	13.058	-0.032	-0.032	0.000	0.000	0.000	0.000
92	A	134	VAL	0	0.017	-0.006	14.340	-0.034	-0.034	0.000	0.000	0.000	0.000
93	A	135	ARG	1	0.881	0.952	9.827	0.224	0.224	0.000	0.000	0.000	0.000
94	A	136	GLY	0	0.064	0.028	10.599	-0.047	-0.047	0.000	0.000	0.000	0.000
95	A	137	SER	0	-0.091	-0.031	9.158	-0.041	-0.041	0.000	0.000	0.000	0.000
96	A	138	ILE	0	0.057	0.049	9.936	0.025	0.025	0.000	0.000	0.000	0.000
97	A	139	ARG	1	0.879	0.931	11.995	0.167	0.167	0.000	0.000	0.000	0.000
98	A	140	THR	0	0.067	0.034	14.983	0.026	0.026	0.000	0.000	0.000	0.000
99	A	141	TYR	0	-0.024	-0.024	18.140	-0.016	-0.016	0.000	0.000	0.000	0.000
100	A	142	ARG	1	0.914	0.956	21.301	0.030	0.030	0.000	0.000	0.000	0.000
101	A	143	GLU	-1	-0.945	-0.967	23.414	0.012	0.012	0.000	0.000	0.000	0.000
102	A	144	GLU	-1	-0.889	-0.916	22.382	0.033	0.033	0.000	0.000	0.000	0.000
103	A	145	ARG	1	0.823	0.885	15.447	-0.118	-0.118	0.000	0.000	0.000	0.000
104	A	146	GLU	-1	-0.875	-0.950	17.217	-0.030	-0.030	0.000	0.000	0.000	0.000
105	A	147	ILE	0	0.007	0.006	12.857	-0.008	-0.008	0.000	0.000	0.000	0.000
106	A	148	HIS	0	-0.075	-0.033	13.849	-0.025	-0.025	0.000	0.000	0.000	0.000
107	A	149	ALA	0	-0.003	-0.004	13.329	-0.039	-0.039	0.000	0.000	0.000	0.000
108	A	150	THR	0	-0.005	-0.023	10.310	0.009	0.009	0.000	0.000	0.000	0.000
109	A	151	THR	0	-0.071	-0.050	13.399	-0.016	-0.016	0.000	0.000	0.000	0.000
110	A	152	TYR	0	-0.005	0.001	15.319	0.019	0.019	0.000	0.000	0.000	0.000
111	A	153	TYR	0	-0.037	-0.014	16.860	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	154	LYS	1	0.967	0.987	21.028	0.023	0.023	0.000	0.000	0.000	0.000
113	A	155	VAL	0	-0.078	-0.055	20.742	-0.005	-0.005	0.000	0.000	0.000	0.000
114	A	156	ASP	-1	-0.895	-0.941	23.789	0.011	0.011	0.000	0.000	0.000	0.000
115	A	157	ASP	-1	-0.758	-0.897	25.415	0.064	0.064	0.000	0.000	0.000	0.000
116	A	158	PRO	0	0.018	0.023	27.394	0.005	0.005	0.000	0.000	0.000	0.000
117	A	159	VAL	0	-0.016	-0.017	30.215	0.000	0.000	0.000	0.000	0.000	0.000
118	A	160	TRP	0	0.020	0.004	27.165	0.003	0.003	0.000	0.000	0.000	0.000
119	A	161	ASN	0	-0.018	0.005	26.125	0.015	0.015	0.000	0.000	0.000	0.000
120	A	162	ILE	0	-0.002	-0.014	20.794	0.013	0.013	0.000	0.000	0.000	0.000
121	A	163	GLN	0	-0.054	-0.041	21.795	0.024	0.024	0.000	0.000	0.000	0.000
122	A	164	ILE	0	0.019	0.018	22.849	0.018	0.018	0.000	0.000	0.000	0.000
123	A	165	ALA	0	0.005	0.004	21.444	0.016	0.016	0.000	0.000	0.000	0.000
124	A	166	ARG	1	0.849	0.913	14.292	-0.178	-0.178	0.000	0.000	0.000	0.000
125	A	167	MET	0	0.003	-0.011	19.150	0.029	0.029	0.000	0.000	0.000	0.000
126	A	168	LEU	0	-0.032	-0.008	21.711	0.013	0.013	0.000	0.000	0.000	0.000
127	A	169	GLU	-1	-0.936	-0.968	15.103	0.341	0.341	0.000	0.000	0.000	0.000
128	A	170	LEU	0	0.014	-0.003	14.612	0.051	0.051	0.000	0.000	0.000	0.000
129	A	171	PRO	0	0.011	0.014	16.714	0.052	0.052	0.000	0.000	0.000	0.000
130	A	172	THR	0	-0.012	-0.003	17.260	0.010	0.010	0.000	0.000	0.000	0.000
131	A	173	ILE	0	-0.033	-0.008	11.638	0.034	0.034	0.000	0.000	0.000	0.000
132	A	174	TYR	0	-0.045	-0.064	13.812	0.127	0.127	0.000	0.000	0.000	0.000
133	A	175	ARG	1	0.969	0.994	15.506	-0.242	-0.242	0.000	0.000	0.000	0.000
134	A	176	LYS	1	0.905	0.946	15.044	-0.416	-0.416	0.000	0.000	0.000	0.000
135	A	177	VAL	0	-0.015	-0.006	9.306	0.026	0.026	0.000	0.000	0.000	0.000
136	A	178	TYR	0	-0.025	-0.011	8.295	0.102	0.102	0.000	0.000	0.000	0.000
137	A	179	ASP	-1	-0.792	-0.906	12.691	0.348	0.348	0.000	0.000	0.000	0.000
138	A	180	GLN	0	-0.094	-0.028	14.706	-0.095	-0.095	0.000	0.000	0.000	0.000
139	A	181	PRO	0	0.013	0.021	14.287	0.064	0.064	0.000	0.000	0.000	0.000
140	A	182	PHE	0	-0.011	-0.015	6.937	0.051	0.051	0.000	0.000	0.000	0.000
141	A	183	HIS	0	-0.012	0.001	7.358	-0.055	-0.055	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:24:LEU)